ID   NCS1_PAPSO              Reviewed;         231 AA.
AC   Q4QTJ2;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=S-norcoclaurine synthase 1 {ECO:0000303|PubMed:15925393};
DE            Short=PsNCS1 {ECO:0000303|PubMed:15925393};
DE            EC=4.2.1.78 {ECO:0000269|PubMed:15925393};
DE   Flags: Precursor;
GN   Name=NCS1 {ECO:0000303|PubMed:15925393};
OS   Papaver somniferum (Opium poppy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Papaver.
OX   NCBI_TaxID=3469 {ECO:0000312|EMBL:AAX56303.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15925393; DOI=10.1016/j.phytochem.2005.04.029;
RA   Liscombe D.K., Macleod B.P., Loukanina N., Nandi O.I., Facchini P.J.;
RT   "Evidence for the monophyletic evolution of benzylisoquinoline alkaloid
RT   biosynthesis in angiosperms.";
RL   Phytochemistry 66:1374-1393(2005).
RN   [2]
RP   TISSUE SPECIFICITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11722126; DOI=10.1007/s004250100581;
RA   Samanani N., Facchini P.J.;
RT   "Isolation and partial characterization of norcoclaurine synthase, the
RT   first committed step in benzylisoquinoline alkaloid biosynthesis, from
RT   opium poppy.";
RL   Planta 213:898-906(2001).
CC   -!- FUNCTION: Involved in the biosynthesis of (S)-coclaurine, the common
CC       precursor of all benzylisoquinoline alkaloids such as morphine,
CC       sanguinarine, codeine or papaverine. Condenses dopamine and 4-
CC       hydroxyphenylacetaldehyde. {ECO:0000269|PubMed:15925393}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4-hydroxyphenyl)acetaldehyde + dopamine = (S)-norcoclaurine +
CC         H2O; Xref=Rhea:RHEA:16173, ChEBI:CHEBI:15377, ChEBI:CHEBI:15621,
CC         ChEBI:CHEBI:58253, ChEBI:CHEBI:59905; EC=4.2.1.78;
CC         Evidence={ECO:0000269|PubMed:15925393};
CC   -!- ACTIVITY REGULATION: Activity doubles within 5 hours of elicitor
CC       treatment and continues to increase for at least 80 hours.
CC       {ECO:0000269|PubMed:11722126}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.02 mM for 4-hydroxyphenylacetaldehyde
CC         {ECO:0000269|PubMed:11722126};
CC         Note=Sigmoidal saturation kinetics suggesting positive cooperativity
CC         in the binding of dopamine. {ECO:0000269|PubMed:11722126};
CC       pH dependence:
CC         Optimum pH is between 6.5 and 7.0. {ECO:0000269|PubMed:11722126};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:11722126};
CC   -!- PATHWAY: Alkaloid biosynthesis; (S)-reticuline biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Detected in roots, stems, leaves, flower buds and
CC       germinating seeds. {ECO:0000269|PubMed:11722126}.
CC   -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
CC   -!- CAUTION: The tissue specificity and the characterization shown in
CC       PubMed:11722126 are from a soluble protein extract not making the
CC       distinction between the two proteins produced by NCS1 and NCS2.
CC       {ECO:0000305}.
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DR   EMBL; AY860500; AAX56303.1; -; mRNA.
DR   AlphaFoldDB; Q4QTJ2; -.
DR   SMR; Q4QTJ2; -.
DR   BRENDA; 4.2.1.78; 4515.
DR   UniPathway; UPA00306; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050474; F:(S)-norcoclaurine synthase activity; IDA:UniProtKB.
DR   GO; GO:1901010; P:(S)-reticuline metabolic process; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IDA:UniProtKB.
DR   Gene3D; 3.30.530.20; -; 1.
DR   InterPro; IPR000916; Bet_v_I/MLP.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   Pfam; PF00407; Bet_v_1; 1.
PE   1: Evidence at protein level;
KW   Alkaloid metabolism; Lyase; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000250|UniProtKB:Q4QTJ1"
FT   CHAIN           ?..231
FT                   /note="S-norcoclaurine synthase 1"
FT                   /id="PRO_0000433979"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        121
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q67A25"
FT   BINDING         107..109
FT                   /ligand="dopamine"
FT                   /ligand_id="ChEBI:CHEBI:59905"
FT                   /evidence="ECO:0000250|UniProtKB:Q67A25"
FT   BINDING         140
FT                   /ligand="(4-hydroxyphenyl)acetaldehyde"
FT                   /ligand_id="ChEBI:CHEBI:15621"
FT                   /evidence="ECO:0000250|UniProtKB:Q67A25"
SQ   SEQUENCE   231 AA;  26015 MW;  96CD8DCAD42474BC CRC64;
     MSKLITTEPL KSMAEVISNY AMKQQSVSER NIPKKQSLLR KEITYETEVQ TSADSIWNVY
     SSPDIPRLLR DVLLPGVFEK LDVIAGNGGV GTVLDIAFPL GAVPRRYKEK FVKINHEKRL
     KEVVMIEGGY LDMGCTFYMD RIHIFEKTPN SCVIESSIIY EVKEEYAGKM AKLITTEPLE
     SMAEVISGYV LKKRLQVFGF EIKPKLRFNL LLCLIICLVI AGGMFVAGVP L